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Abstract:

Methods previously described for glycogen or amylopectin branching enzymatic activity are insufficiently sensitive and not quantitative. A new, more sensitive, specific, and quantitative one was developed. It is based upon the quantitation of the glucose residues joined by α1,6 bonds introduced by varying amounts of branching enzyme. The procedure involved the synthesis of a polysaccharide from Glc-1-P and phosphorylase in the presence of the sample to be tested. The branched polysaccharide was then purified and the glucoses involved in the branching points were quantitated after degradation with phosphorylase and debranching enzymes. This method appeared to be useful, not only in enzymatic activity determinations but also in the study of the structure of α-d-glucans when combined with those of total polysaccharide quantitation, such as iodine and phenol-sulfuric acid. © 1985.

Registro:

Documento: Artículo
Título:Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points
Autor:Krisman, C.R.; Tolmasky, D.S.; Raffo, S.
Filiación:Instituto de Investigaciones Bioquimicas Fundacion Campomar Antonio Machado 151, 1405 Buenos Aires, Argentina
Facultad de Ciencias Exactas y Naturales, Antonio Machado 151, 1405 Buenos Aires, Argentina
Palabras clave:amylo-α1,4-α1,6-transglucosylase; amylopectin; branching enzyme assay; glycogen; quantitation of branching points; α1,6-glucosydic linkage; 1,4 alpha glucan branching enzyme; enzyme assay; nonhuman; priority journal; 1,4-alpha-Glucan Branching Enzyme; Animal; Glucans; Glucosyltransferases; Polysaccharides; Rabbits
Año:1985
Volumen:147
Número:2
Página de inicio:491
Página de fin:496
DOI: http://dx.doi.org/10.1016/0003-2697(85)90303-3
Título revista:Analytical Biochemistry
Título revista abreviado:Anal. Biochem.
ISSN:00032697
CODEN:ANBCA
CAS:1,4 alpha glucan branching enzyme, 9001-97-2; 1,4-alpha-Glucan Branching Enzyme, EC 2.4.1.18; Glucans; Glucosyltransferases, EC 2.4.1.-; Polysaccharides
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00032697_v147_n2_p491_Krisman

Referencias:

  • Boyer, Preiss, Multiple forms of (1 → 4)-α-d-glucan, (1 → 4)-α-d-glucan-6- glycosyl transferase from developing zea mays L. Kernels (1978) Carbohydrate Research, 61, p. 321
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Citas:

---------- APA ----------
Krisman, C.R., Tolmasky, D.S. & Raffo, S. (1985) . Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points. Analytical Biochemistry, 147(2), 491-496.
http://dx.doi.org/10.1016/0003-2697(85)90303-3
---------- CHICAGO ----------
Krisman, C.R., Tolmasky, D.S., Raffo, S. "Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points" . Analytical Biochemistry 147, no. 2 (1985) : 491-496.
http://dx.doi.org/10.1016/0003-2697(85)90303-3
---------- MLA ----------
Krisman, C.R., Tolmasky, D.S., Raffo, S. "Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points" . Analytical Biochemistry, vol. 147, no. 2, 1985, pp. 491-496.
http://dx.doi.org/10.1016/0003-2697(85)90303-3
---------- VANCOUVER ----------
Krisman, C.R., Tolmasky, D.S., Raffo, S. Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points. Anal. Biochem. 1985;147(2):491-496.
http://dx.doi.org/10.1016/0003-2697(85)90303-3